Crystal Structures of Glycosyltransferase UGT78G1 Reveal the Molecular Basis for Glycosylation and Deglycosylation of (Iso)flavonoids
Crystal Structures of Glycosyltransferase UGT78G1 Reveal the Molecular Basis for Glycosylation and Deglycosylation of (Iso)flavonoids
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DOI：
10.1016/j.jmb.2009.08.017
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发表时间：
2009-10-09
影响因子：
5.6
通讯作者：
Wang, Xiaoqiang
中科院分区：
文献类型：
--
作者：
Modolo, Luzia V.;Li, Lenong;Wang, Xiaoqiang
来自蒺藜苜蓿（Medicago truncatula）的糖基转移酶UGT 78 G1催化各种（异）黄酮类化合物的糖基化，所述黄酮类化合物例如黄酮醇类山奈酚和杨梅素、刺芒柄花黄素以及花色素天竺葵色素和矢车菊色素。它还催化从糖苷中除去糖部分的逆反应。在2.1埃分辨率下测定了与尿苷二磷酸或与尿苷二磷酸和杨梅苷结合的UGT 78 G1的结构，揭示了酶与底物/产物之间的详细相互作用，并表明受体/产物的独特结合模式。比较结构分析和诱变鉴定谷氨酸192作为逆反应的关键氨基酸。这些信息为酶工程提供了基础，以操纵底物特异性，并设计有效的生物催化剂与糖基化和/或cleglycosylation活性。(C)2009爱思唯尔有限公司保留所有权利。
The glycosyltransferase UGT78G1 from Medicago truncatula catalyzes the glycosylation of various (iso)flavonoids such as the flavonols kaempferol and myricetin, the isoflavone formononetin, and the anthocyanidins pelargonidin and cyanidin. It also catalyzes a reverse reaction to remove the sugar moiety from glycosides. The structures of UGT78G1 bound with uridine diphosphate or with both uridine diphosphate and myricetin were determined at 2.1 angstrom resolution, revealing detailed interactions between the enzyme and substrates/products and suggesting a distinct binding mode for the acceptor/product. Comparative structural analysis and mutagenesis identify glutamate 192 as a key amino acid for the reverse reaction. This information provides a basis for enzyme engineering to manipulate substrate specificity and to design effective biocatalysts with glycosylation and/or cleglycosylation activity. (C) 2009 Elsevier Ltd. All rights reserved.